Is EGFR a receptor tyrosine kinase?

The epidermal growth factor receptor (EGFR) is often considered the “prototypical” receptor tyrosine kinase (RTK) and has been intensively studied. It is one of a family of four RTKs in humans, the others being ErbB2/HER2, ErbB3/HER3, and ErbB4/HER4 (Fig.

Where is EGFR phosphorylated?

3.4. In this multimolecular complex, EGFR is phosphorylated in an EGF-independent manner on Y845, Y1068, Y1086, and Y1173, but not on Y1148, a major autophosphorylation site.

What happens when EGF binds to EGFR?

Upon ligand binding to the extracellular domain of EGFR, its transmembrane domains rotate or twist parallel to the plane of the cell membrane, resulting in the reorientation of the intracellular kinase domain dimer from a symmetric inactive configuration to an asymmetric active form (the “rotation model”).

What is the structure of EGFR?

The epidermal growth factor receptor (EGFR) is a single-chain transmembrane protein comprised of an extracellular EGF-binding domain, a short transmembrane sequence, and a cytoplasmic region that incorporates a protein tyrosine kinase domain and a C-terminal phosphorylation domain.

What kind of receptors is EGFR?

Epidermal growth factor receptors are a type of receptor tyrosine kinase. Also called EGFR, ErbB1, and HER1.

What does the EGFR do?

Normal Function The EGFR gene provides instructions for making a receptor protein called the epidermal growth factor receptor, which spans the cell membrane so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell.

What does phosphorylated EGFR do?

Activated EGFR (phosphorylated EGFR [pEGFR]) stimulates a number of different signal transduction pathways, such as the Ras/mitogen-activated protein kinase pathway, the phosphoinositide-3 kinase (PI3K)/Akt pathway and the phospholipase-Cγ/protein kinase C pathway.

How is EGFR inactivated?

A second mechanism by which EGFRs are inactivated is the catalyzed dephosphorylation of the receptor by phosphatases. The discovery of protein-tyrosine phosphatases (PTP) came several years after that of tyrosine kinases, but they were immediately recognized as important regulatory components of signaling (Tonks et al.